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Conserved domains on  [gi|548960717|ref|NP_001271457|]
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zinc finger and SCAN domain-containing protein 32 isoform c [Homo sapiens]

Protein Classification

Myb_DNA-bind_4 and COG5048 domain-containing protein( domain architecture ID 12155611)

Myb_DNA-bind_4 and COG5048 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
 1-45 4.00e-10

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.


:

Pssm-ID: 463994  Cd Length: 84  Bit Score: 56.12  E-value: 4.00e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 548960717    1 MAEGLWEQGFLRTPEQCRTKFKSLQLSYRKVRRGRV--PEPCIFYEE 45
Cdd:pfam13837  38 IAEKMAELGYNRSPEQCKEKWENLKKKYRKEKEGNNgsGSSWPFFEE 84
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
230-379 6.90e-10

FOG: Zn-finger [General function prediction only];


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.48  E-value: 6.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548960717 230 KVSQCPECGKTFSRSSYLVRHQR--IHTGE--KPHKCSE--CGKGFSERSNLTAHLRTHTGERPYQC--GQCGKSFNQSS 301
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548960717 302 -----SLIVHQRTHTGEKPYQCIV--CGKRFNNSSQFSAHRRIHTGESP--YKCAVCGKIFNNSSHFSAHRKTHTGEKPY 372
Cdd:COG5048  368 nneppQSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPL 447


                 ....*..
gi 548960717 373 RCSHCER 379
Cdd:COG5048  448 LCSILKS 454
 
Name Accession Description Interval E-value
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
 1-45 4.00e-10

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.


Pssm-ID: 463994  Cd Length: 84  Bit Score: 56.12  E-value: 4.00e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 548960717    1 MAEGLWEQGFLRTPEQCRTKFKSLQLSYRKVRRGRV--PEPCIFYEE 45
Cdd:pfam13837  38 IAEKMAELGYNRSPEQCKEKWENLKKKYRKEKEGNNgsGSSWPFFEE 84
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
230-379 6.90e-10

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.48  E-value: 6.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548960717 230 KVSQCPECGKTFSRSSYLVRHQR--IHTGE--KPHKCSE--CGKGFSERSNLTAHLRTHTGERPYQC--GQCGKSFNQSS 301
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548960717 302 -----SLIVHQRTHTGEKPYQCIV--CGKRFNNSSQFSAHRRIHTGESP--YKCAVCGKIFNNSSHFSAHRKTHTGEKPY 372
Cdd:COG5048  368 nneppQSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPL 447


                 ....*..
gi 548960717 373 RCSHCER 379
Cdd:COG5048  448 LCSILKS 454
zf-H2C2_2 pfam13465
Zinc-finger double domain;
246-270 2.47e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 2.47e-05
                          10        20
                  ....*....|....*....|....*
gi 548960717  246 YLVRHQRIHTGEKPHKCSECGKGFS 270
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 286-334 1.78e-03

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 37.15  E-value: 1.78e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 548960717 286 RPYqCGQCGKSFNQSSSLIVHQRTHTgekpYQCIVCGKRFNNSSQFSAH 334
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
GT1 cd12203
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
 2-32 4.49e-03

GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription factors. GT-1 binds the GT cis-element of rbcS-3A, a light-induced gene, as a dimer. Arabidopsis GT-1 is a trans-activator and acts in the stabilization of components of the transcription pre-initiation complex comprised of TFIIA-TBP-TATA. The isolated GT-1 DNA-binding domain is sufficient to bind DNA. This region closely resembles the myb domain, but with longer helices. It has been proposed that GT-1 may respond to light signals via calcium-dependent phosphorylation to create a light-modulated molecular switch. These proteins are members of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of the DNA-binding Myb domains and is found in a diverse set of proteins.


Pssm-ID: 213402  Cd Length: 66  Bit Score: 35.33  E-value: 4.49e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 548960717   2 AEGLWEQGFLRTPEQCRTKFKSLQLSYRKVR 32
Cdd:cd12203   36 AAKMRELGYNRSAKQCKEKWENLNKYYKKVK 66
 
Name Accession Description Interval E-value
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
 1-45 4.00e-10

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.


Pssm-ID: 463994  Cd Length: 84  Bit Score: 56.12  E-value: 4.00e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 548960717    1 MAEGLWEQGFLRTPEQCRTKFKSLQLSYRKVRRGRV--PEPCIFYEE 45
Cdd:pfam13837  38 IAEKMAELGYNRSPEQCKEKWENLKKKYRKEKEGNNgsGSSWPFFEE 84
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
230-379 6.90e-10

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 60.48  E-value: 6.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548960717 230 KVSQCPECGKTFSRSSYLVRHQR--IHTGE--KPHKCSE--CGKGFSERSNLTAHLRTHTGERPYQC--GQCGKSFNQSS 301
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548960717 302 -----SLIVHQRTHTGEKPYQCIV--CGKRFNNSSQFSAHRRIHTGESP--YKCAVCGKIFNNSSHFSAHRKTHTGEKPY 372
Cdd:COG5048  368 nneppQSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPL 447


                 ....*..
gi 548960717 373 RCSHCER 379
Cdd:COG5048  448 LCSILKS 454
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
220-302 1.40e-07

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.16  E-value: 1.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548960717 220 SPHKPALKLEKVSQCPECGKTFSRSSYLVRHQRIHTGEKPHKCS--ECGKGFSERSNLTAHLRTHTGERPYQCGQCGKSF 297
Cdd:COG5048   22 STLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLS 101


                 ....*
gi 548960717 298 NQSSS 302
Cdd:COG5048  102 NSKAS 106
zf-H2C2_2 pfam13465
Zinc-finger double domain;
246-270 2.47e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 2.47e-05
                          10        20
                  ....*....|....*....|....*
gi 548960717  246 YLVRHQRIHTGEKPHKCSECGKGFS 270
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
302-327 4.90e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 4.90e-05
                          10        20
                  ....*....|....*....|....*.
gi 548960717  302 SLIVHQRTHTGEKPYQCIVCGKRFNN 327
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
274-299 7.46e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 7.46e-05
                          10        20
                  ....*....|....*....|....*.
gi 548960717  274 NLTAHLRTHTGERPYQCGQCGKSFNQ 299
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 256-335 1.25e-04

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.94  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548960717 256 GEKPHKCS--ECGKGFSERSNLTAHlRTHtgerpyqcGQCGKSFNQSSSLIVHQRTHTGEKPYQCIVCGKRFNNSSQFSA 333
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 ..
gi 548960717 334 HR 335
Cdd:COG5189  417 HR 418
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
205-362 2.00e-04

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.53  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548960717 205 CTHILCGKNCSQ-SVHSPHKPALKLE----KVSQCPE--CGKTFSRSSYLVRHQRIHTGEKPHKCSECGKGFSERSNLTA 277
Cdd:COG5048  290 IKSKQCNISFSRsSPLTRHLRSVNHSgeslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNN 369

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548960717 278 -----------HLRTHTGERPYQCgqCGKSFNQSSSLIVHQRTHTGEKPYQC--IVCGKRFNNSSQFSAHRRIHTGESPY 344
Cdd:COG5048  370 eppqslqqykdLKNDKKSETLSNS--CIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPL 447

                        170
                 ....*....|....*...
gi 548960717 345 KCAVCGKiFNNSSHFSAH 362
Cdd:COG5048  448 LCSILKS-FRRDLDLSNH 464
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 233-254 2.05e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.05  E-value: 2.05e-04
                          10        20
                  ....*....|....*....|..
gi 548960717  233 QCPECGKTFSRSSYLVRHQRIH 254
Cdd:pfam00096   2 KCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
286-347 3.18e-04

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.76  E-value: 3.18e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548960717 286 RPYQCGQCGKSFNQSSSLIVHQRTHTGEKPYQCIV--CGKRFNNSSQFSAHRRIHTGESPYKCA 347
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNS 95
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 288-310 3.62e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.28  E-value: 3.62e-04
                          10        20
                  ....*....|....*....|...
gi 548960717  288 YQCGQCGKSFNQSSSLIVHQRTH 310
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 260-282 5.51e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.89  E-value: 5.51e-04
                          10        20
                  ....*....|....*....|...
gi 548960717  260 HKCSECGKGFSERSNLTAHLRTH 282
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
258-395 6.34e-04

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.99  E-value: 6.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548960717 258 KPHKCSECGKGFSERSNLTAHLRTHTGERPYQCGQ--CGKSFNQSSSLIVHQRTHTGEKPYQCIVCGKRFNNSSQFSAHR 335
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548960717 336 RIHTgESPYKCAVCGKIFNNSSHFSAHR----KTHTGEKPYRCSHCERGFTKNSALTRHQTVHM 395
Cdd:COG5048  112 SSSS-NSNDNNLLSSHSLPPSSRDPQLPdllsISNLRNNPLPGNNSSSVNTPQSNSLHPPLPAN 174
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 286-334 1.78e-03

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 37.15  E-value: 1.78e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 548960717 286 RPYqCGQCGKSFNQSSSLIVHQRTHTgekpYQCIVCGKRFNNSSQFSAH 334
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 344-366 3.35e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.58  E-value: 3.35e-03
                          10        20
                  ....*....|....*....|...
gi 548960717  344 YKCAVCGKIFNNSSHFSAHRKTH 366
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
334-355 3.46e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 3.46e-03
                          10        20
                  ....*....|....*....|..
gi 548960717  334 HRRIHTGESPYKCAVCGKIFNN 355
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
GT1 cd12203
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
 2-32 4.49e-03

GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription factors. GT-1 binds the GT cis-element of rbcS-3A, a light-induced gene, as a dimer. Arabidopsis GT-1 is a trans-activator and acts in the stabilization of components of the transcription pre-initiation complex comprised of TFIIA-TBP-TATA. The isolated GT-1 DNA-binding domain is sufficient to bind DNA. This region closely resembles the myb domain, but with longer helices. It has been proposed that GT-1 may respond to light signals via calcium-dependent phosphorylation to create a light-modulated molecular switch. These proteins are members of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of the DNA-binding Myb domains and is found in a diverse set of proteins.


Pssm-ID: 213402  Cd Length: 66  Bit Score: 35.33  E-value: 4.49e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 548960717   2 AEGLWEQGFLRTPEQCRTKFKSLQLSYRKVR 32
Cdd:cd12203   36 AAKMRELGYNRSAKQCKEKWENLNKYYKKVK 66
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 312-392 5.69e-03

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 38.55  E-value: 5.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548960717 312 GEKPYQCIV--CGKRFNNSSQFSAHRrIHTGESPYKCAVCGKIFNNSshFSAHrkthtgEKPYRCSHCERGFTKNSALTR 389
Cdd:COG5189  346 DGKPYKCPVegCNKKYKNQNGLKYHM-LHGHQNQKLHENPSPEKMNI--FSAK------DKPYRCEVCDKRYKNLNGLKY 416


                 ...
gi 548960717 390 HQT 392
Cdd:COG5189  417 HRK 419
zf-H2C2_2 pfam13465
Zinc-finger double domain;
362-383 8.55e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.50  E-value: 8.55e-03
                          10        20
                  ....*....|....*....|..
gi 548960717  362 HRKTHTGEKPYRCSHCERGFTK 383
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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